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Phosphatidylinositol phosphate binds KCNQ1. 14 / 14
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"Out of 27 KCNQ1 predicted binding clusters in the KCNQ1-PIP 2 -calmodulin/KCNE3 structure, the top three in terms of most negative ΔG values (−8.75, −8.26 and −7.82 kJ/mol) positioned quercetin close to and/or H-binding with the R231 sidechain (Fig.  xref )."
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"We previously identified a cluster of basic residues in the proximal C-terminus of KCNQ1 that form a PIP 2 /phosphoinositide binding site."
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"Some Long QT mutations of KCNQ1, including R243H, R539W and R555C have been shown to decrease KCNQ1 interaction with PIP 2 ."
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"Regarding KCNQ1, we have shown that type 1 long QT (LQT1) syndrome can be associated with a decrease in KCNQ1-PIP 2 interactions provoked by mutations in the S4–S5 linker (R243H) and in the C-terminal domain CTD (R539W and R555C) xref ."
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"Among all lipids, four PIP 2 molecules interacted with several positive residues of Kv7.1 simultaneously, consistent with strong binding of PIP 2 to the channel."
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"Quercetin also docked to the top of the VSD in the cryo-EM-derived structure of human KCNQ1-PIP 2 -calmodulin/KCNE3 xref , notably being predicted to H-bond to the R231 sidechain."
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"Some LQTS associated mutations (R539W and R555C) might weaken the interaction between KCNQ1 and KCNE1 and PIP 2 and therefore destabilize the PIP 2 -mediated open state of KCNQ1 and KCNE1 channels [XREF_BIBR]."
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"As a result, both novel structures and states have been observed, with many cryo-EM structures of membrane proteins revealing lipids, including phosphatidylglycerol (PG), cholesterol, PIP and phosphatidylinositol (PI), bound to the structures.10Recent cryo-EM structures of the KCNQ1 and K 3.2 channels have captured binding sites for PIP ."
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"It is not yet known whether KCNE3 has similar effects, but all members of the KCNE family possess similar residues to those important for modifying the manner in which PIP 2 interacts with KCNQ1 60."
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"Thus, for R366Q and R555C mutant channels, regulation of the channel by PIP 2 was potentiated, suggesting that PKA and PKC activate the channel by strengthening KCNQ1 interactions with PIP 2 ."
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"It is not yet known whether KCNE3 has similar effects, but all members of the KCNE family possess similar residues to those important for modifying the manner in which PIP 2 interacts with KCNQ1 (Li e[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Analyzing the average number of salt bridges for prolonged trajectories (additional 20 and 40 ns), we have found similar interactions between Kv7.1 and PIP 2 (see xref ), indicating that the performed simulations have converged within the 100 ns time scale."
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"Interestingly, it has been suggested that PIP and CaM binding sites within the Kv7 channels overlap (Delmas and Brown, 2005; Haitin and Attali, 2008), accordingly, binding of PIP and PIP to Kv7.1 have been shown to compete against CaM (Kwon et al., 2007)."
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"It is thought that increases in cytosolic Ca 2+ can compensate for receptor-mediated depletion of PIP 2 via an interaction between the calcified N lobe of CaM and the KCNQ1 proximal C-terminus (at Helix B) that mimics or substitutes for the KCNQ1-PIP 2 interaction to curtail I Ks current inhibition ( xref )."
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